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- W2984975897 abstract "Tumor cells rely on glycolysis to meet their elevated demand for energy. Thereby they produce significant amounts of lactate and protons, which are exported via monocarboxylate transporters (MCTs), supporting the formation of an acidic microenvironment. The present study demonstrates that carbonic anhydrase IX (CAIX), one of the major acid/base regulators in cancer cells, forms a protein complex with MCT1 and MCT4 in tissue samples from human breast cancer patients, but not healthy breast tissue. Formation of this transport metabolon requires binding of CAIX to the Ig1 domain of the MCT1/4 chaperon CD147 and is required for CAIX-mediated facilitation of MCT1/4 activity. Application of an antibody, directed against the CD147-Ig1 domain, displaces CAIX from the transporter and suppresses CAIX-mediated facilitation of proton-coupled lactate transport. In cancer cells, this “metabolon disruption” results in a decrease in lactate transport, reduced glycolysis, and ultimately reduced cell proliferation. Taken together, the study shows that carbonic anhydrases form transport metabolons with acid/base transporters in human tumor tissue and that these interactions can be exploited to interfere with tumor metabolism and proliferation." @default.
- W2984975897 created "2019-11-22" @default.
- W2984975897 creator A5054738613 @default.
- W2984975897 creator A5071807487 @default.
- W2984975897 creator A5079118082 @default.
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- W2984975897 date "2019-11-13" @default.
- W2984975897 modified "2023-10-02" @default.
- W2984975897 title "CAIX forms a transport metabolon with monocarboxylate transporters in human breast cancer cells" @default.
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- W2984975897 doi "https://doi.org/10.1038/s41388-019-1098-6" @default.
- W2984975897 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31723238" @default.
- W2984975897 hasPublicationYear "2019" @default.
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